(data stored in SCRATCH zone)

SWISSPROT: A5GRQ3_SYNR3

ID   A5GRQ3_SYNR3            Unreviewed;       508 AA.
AC   A5GRQ3;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   13-FEB-2019, entry version 69.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit 2 {ECO:0000256|HAMAP-Rule:MF_00445};
DE            EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_00445};
DE   AltName: Full=NAD(P)H dehydrogenase subunit 2 {ECO:0000256|HAMAP-Rule:MF_00445};
DE   AltName: Full=NADH-plastoquinone oxidoreductase subunit 2 {ECO:0000256|HAMAP-Rule:MF_00445};
DE   AltName: Full=NDH-1, subunit 2 {ECO:0000256|HAMAP-Rule:MF_00445};
GN   Name=ndhB {ECO:0000256|HAMAP-Rule:MF_00445,
GN   ECO:0000313|EMBL:CAK27562.1};
GN   OrderedLocusNames=SynRCC307_0659 {ECO:0000313|EMBL:CAK27562.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27562.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NDH-1 shuttles electrons from an unknown electron donor,
CC       via FMN and iron-sulfur (Fe-S) centers, to quinones in the
CC       respiratory and/or the photosynthetic chain. The immediate
CC       electron acceptor for the enzyme in this species is believed to be
CC       plastoquinone. Couples the redox reaction to proton translocation,
CC       and thus conserves the redox energy in a proton gradient.
CC       Cyanobacterial NDH-1 also plays a role in inorganic carbon-
CC       concentration. {ECO:0000256|HAMAP-Rule:MF_00445}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol
CC         + n H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-
CC         COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17757, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:62192; Evidence={ECO:0000256|HAMAP-Rule:MF_00445};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol
CC         + n H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-
CC         COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17757, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:62192; Evidence={ECO:0000256|HAMAP-Rule:MF_00445};
CC   -!- SUBUNIT: NDH-1 can be composed of about 15 different subunits;
CC       different subcomplexes with different compositions have been
CC       identified which probably have different functions.
CC       {ECO:0000256|HAMAP-Rule:MF_00445}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC       {ECO:0000256|HAMAP-Rule:MF_00445}; Multi-pass membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_00445}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 2 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00445}.
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DR   EMBL; CT978603; CAK27562.1; -; Genomic_DNA.
DR   RefSeq; WP_011935077.1; NC_009482.1.
DR   STRING; 316278.SynRCC307_0659; -.
DR   EnsemblBacteria; CAK27562; CAK27562; SynRCC307_0659.
DR   KEGG; syr:SynRCC307_0659; -.
DR   eggNOG; ENOG4105CNR; Bacteria.
DR   eggNOG; COG1007; LUCA.
DR   HOGENOM; HOG000100794; -.
DR   KO; K05573; -.
DR   OMA; QAGFVMI; -.
DR   OrthoDB; 1664448at2; -.
DR   BioCyc; SSP316278:G1GJL-652-MONOMER; -.
DR   Proteomes; UP000001115; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00445; NDH1_NuoN_1; 1.
DR   InterPro; IPR010096; NADH-Q_OxRdtase_suN/2.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   TIGRFAMs; TIGR01770; NDH_I_N; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5GRQ3.
DR   SWISS-2DPAGE; A5GRQ3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00445};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00445};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00445};
KW   Oxidoreductase {ECO:0000313|EMBL:CAK27562.1};
KW   Plastoquinone {ECO:0000256|HAMAP-Rule:MF_00445};
KW   Quinone {ECO:0000256|HAMAP-Rule:MF_00445};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
KW   Thylakoid {ECO:0000256|HAMAP-Rule:MF_00445};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_00445};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00445};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00445};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_00445}.
FT   TRANSMEM     12     33       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00445}.
FT   TRANSMEM     40     60       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00445}.
FT   TRANSMEM     80    100       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00445}.
FT   TRANSMEM    107    124       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00445}.
FT   TRANSMEM    130    150       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00445}.
FT   TRANSMEM    162    185       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00445}.
FT   TRANSMEM    197    221       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00445}.
FT   TRANSMEM    242    264       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00445}.
FT   TRANSMEM    276    295       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00445}.
FT   TRANSMEM    302    319       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00445}.
FT   TRANSMEM    325    350       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00445}.
FT   TRANSMEM    371    400       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00445}.
FT   TRANSMEM    406    426       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00445}.
FT   TRANSMEM    462    485       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00445}.
FT   DOMAIN      127    420       Proton_antipo_M. {ECO:0000259|Pfam:
FT                                PF00361}.
SQ   SEQUENCE   508 AA;  53446 MW;  AA10B9B41113D24C CRC64;
     MESLAQSLNA GAIAPEAAIL IALLACLLAD LAGERTAARL VPPFCYVGLG TSLVLLALQW
     SEPTADAFFS SFITDNLGVA FRAVVATSTL LSLLISWRYV ERAGTPVGEY AAILMAATVG
     AMLLCGATDL VSIFVALETL SVSSYLLSGY MKRDARSSEA ALKYLLVGSA AAAVFLYGTS
     LLYGVSGGST NLDAITISLQ GAGVTPLSAL ALVFVLATVA FKISAVPFHQ WTPDVYEGSP
     TPVVAFLSVG SKAAGFALAL RLLVGCFESF QTQWQLLFTV LAVLSMTLGN VVALAQTSMK
     RMLAYSSIGQ AGFVMIGLVC GTEEGFAAMV LYMAAYLFMN LGAFACVILF SLRTGSDRIS
     DYAGLYQKDP LITLGLSLCL LSLGGIPPML GFFSKIYLFF AGWADGQYLL VVVGLVTSVV
     SIYYYISVIK MMVVKEPQEA SDVIKDYPAP TWNLPGLQPL RAALVFCVAV TAIGGVLSNP
     LFTWANAAVE GTPLLQQVIS NGGHLPTG
//

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